Abstract
Human glycodelin A (GdA) is a glycoprotein that is highly homologous to bovine β-lactoglobulin A (β-LgA) because the amino acid sequences are 50–60% identical. The structural characteristics of human GdA and β-LgA were compared in water and 2-propanol/water solutions. Circular dichroism spectra reveal that in water the two proteins have a very similar β-sheet secondary structure. In the presence of 2-propanol/water mixtures (up to 50% v/v) the α-helix structure of both proteins increases. A further increase in the alcohol percentage of the solvent (up to 80% v/v 2-propanol) causes the formation of a new folded tertiary structure containing mainly β-sheet features. Synchrotron radiation small angle X-ray scattering indicates that, in a neutral pH aqueous solution, GdA is a dimer. Its radius of gyration value ( R g), 25.1±0.4 Å, is greater than that of β-LgA (21.1±0.3 Å), probably because of the contribution of polysaccharides bound to Asn-28 and Asn-63 residues of GdA. Conversely, small angle X-ray scattering and gel permeation chromatography data on GdA in 2-propanol have revealed a massive aggregation of the protein.
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